Researchers at the University of Alberta have developed a novel process to purify very hydrophobic elastin-like polypeptides (ELP). The method enables the expression and purification of ELPs that are poorly expressed and/or have very low transition temperatures. It uses denaturing metal affinity chromatography to recover ELPs from insoluble cell debris and pre-concentrate the target peptides prior to purification by inverse temperature cycling.
Elastin-like polypeptides are comprised of repeating peptide units of VPGXG, wherein the amino acid in the X position can be variable. The nature of the variable amino acid modulates the hydrophobicity of the biopolymer and its general properties. In response to changes in temperature, pH, and ionic strength, ELPs can underdo a reversible phase transition and shift between a linear, disordered state and a more aggregated, ordered state. Due to this unique transition property, the use of ELPs are being explored in a number of applications including customizable drug delivery vehicles, tissue regeneration, biosensor technology, and nanoparticles for specific therapeutic application, among others. However, high-yield purification of recombinantly-produced ELPs has typically been the largest barrier in their production, in particular for extremely hydrophobic ELPs, such as those containing valine or leucine at the variable amino acid position; these desirable polymers typically have low transition temperatures and are very prone to aggregation. Standard protein purification methods are often inadequate or nearly impossible for such hydrophobic ELPs and our method aims to overcome such difficulties to expand the potential use of ELPs.
- The novel method is low-labor intensive and is efficient in purifying insoluble short ELPs.
- Significant cost savings.
- The purified ELPs have applications in targeted drug delivery, tissue regeneration and can be utilized as a research tool.
We are seeking biopharmaceutical partners for collaborative development and licensing
Technology Management Group
TEC Edmonton – University of Alberta